TABLE 3.
Overall comparisons of cyclodextrin-hydrolyzing enzyme, PFTA, and α-amylasea
| ThMA | PFTA | BSTA | |
|---|---|---|---|
| Action mode | Maltose from reducing end | Random | Random |
| Major product(s) from: | |||
| Maltooligosaccharide | G2 | G3, G4 | G2≈G5 |
| Pullulan | Panose | Panose | N.D. |
| β-Cyclodextrin | G2 | G7 | N.D. |
| Acarbose | PTS | PTS | N.D. |
| Length of N-terminal domain (amino acids) | 124 | 196 | N.A. |
| Oligomeric state | Dimer | Dimer | Monomer |
| Optimal temp (°C) | 60 | 90 | 80 |
| Optimal pH | 6.0 | 4.5 | 5.5 |
a
ThMA, maltogenic amylase from Thermus sp. strain IM6501; PFTA, thermostable amylase from P. furiosus, BSTA, thermostable α-amylase from B. stearothermophilus (29). N.D., not detected; N.A., not available.